Literature summary for 2.7.7.23 extracted from

Trempe, J.F.; Shenker, S.; Kozlov, G.; Gehring, K.
Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coli (2011), Protein Sci., 20, 745-752.

Search for more literature for 2.7.7.23

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ACC7	-	-

Subunits

Subunits	Comment	Organism
hexamer	trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction	Escherichia coli
trimer	trimer/hexamer equilibrium, sedimentation equilibrium analytical ultracentrifugation. Two trimers assemble through their N-terminal domains. The interaction is mediated by a loop that undergoes a large conformational change in the uridyl transferase reaction	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)